ID   VL1_HPV1                Reviewed;         508 AA.
AC   P03099;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   23-FEB-2022, entry version 104.
DE   RecName: Full=Major capsid protein L1 {ECO:0000255|HAMAP-Rule:MF_04002};
GN   Name=L1 {ECO:0000255|HAMAP-Rule:MF_04002};
OS   Human papillomavirus type 1 (Human papillomavirus type 1a).
OC   Viruses; Monodnaviria; Shotokuvirae; Cossaviricota; Papovaviricetes;
OC   Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae;
OC   Mupapillomavirus.
OX   NCBI_TaxID=10583;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6325156; DOI=10.1002/j.1460-2075.1982.tb01152.x;
RA   Danos O., Katinka M., Yaniv M.;
RT   "Human papillomavirus 1a complete DNA sequence: a novel type of genome
RT   organization among papovaviridae.";
RL   EMBO J. 1:231-236(1982).
RN   [2]
RP   SEQUENCE REVISION.
RA   Danos O.;
RL   Submitted (JAN-1985) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Forms an icosahedral capsid with a T=7 symmetry and a 50 nm
CC       diameter. The capsid is composed of 72 pentamers linked to each other
CC       by disulfide bonds and associated with L2 proteins. Binds to heparan
CC       sulfate proteoglycans on cell surface of basal layer keratinocytes to
CC       provide initial virion attachment. This binding mediates a
CC       conformational change in the virus capsid that facilitates efficient
CC       infection. The virion enters the host cell via endocytosis. During
CC       virus trafficking, L1 protein dissociates from the viral DNA and the
CC       genomic DNA is released to the host nucleus. The virion assembly takes
CC       place within the cell nucleus. Encapsulates the genomic DNA together
CC       with protein L2. {ECO:0000255|HAMAP-Rule:MF_04002}.
CC   -!- SUBUNIT: Self-assembles into homopentamers. The capsid has an
CC       icosahedral symmetry and consists of 72 capsomers, with each capsomer
CC       being a pentamer of L1. Interacts with the minor capsid protein L2;
CC       this interaction is necessary for viral genome encapsidation. Interacts
CC       with protein E2; this interaction enhances E2-dependent replication and
CC       transcription activation. {ECO:0000255|HAMAP-Rule:MF_04002}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04002}. Host
CC       nucleus {ECO:0000255|HAMAP-Rule:MF_04002}.
CC   -!- SIMILARITY: Belongs to the papillomaviridae L1 protein family.
CC       {ECO:0000255|HAMAP-Rule:MF_04002}.
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DR   EMBL; V01116; CAA24318.1; -; Genomic_DNA.
DR   PIR; A03637; P1WL.
DR   RefSeq; NP_040309.1; NC_001356.1.
DR   SMR; P03099; -.
DR   PRIDE; P03099; -.
DR   GeneID; 1489173; -.
DR   KEGG; vg:1489173; -.
DR   Proteomes; UP000006372; Genome.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0039620; C:T=7 icosahedral viral capsid; IEA:UniProtKB-UniRule.
DR   GO; GO:0005198; F:structural molecule activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0075509; P:endocytosis involved in viral entry into host cell; IEA:UniProtKB-KW.
DR   GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.60.175.20; -; 2.
DR   HAMAP; MF_04002; PPV_L1; 1.
DR   InterPro; IPR002210; Capsid_L1_Papillomavir.
DR   InterPro; IPR036973; Capsid_L1_sf_Papillomavir.
DR   InterPro; IPR011222; dsDNA_vir_gr_I_capsid.
DR   Pfam; PF00500; Late_protein_L1; 1.
DR   PRINTS; PR00865; HPVCAPSIDL1.
DR   SUPFAM; SSF88648; SSF88648; 1.
PE   3: Inferred from homology;
KW   Capsid protein; Disulfide bond; Host nucleus; Host-virus interaction;
KW   Late protein; Reference proteome; T=7 icosahedral capsid protein;
KW   Viral attachment to host cell; Viral penetration into host cytoplasm;
KW   Virion; Virus endocytosis by host; Virus entry into host cell.
FT   CHAIN           1..508
FT                   /note="Major capsid protein L1"
FT                   /id="PRO_0000133483"
FT   REGION          480..508
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        480..496
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        179
FT                   /note="Interchain (with C-435)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
FT   DISULFID        435
FT                   /note="Interchain (with C-179)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04002"
SQ   SEQUENCE   508 AA;  57634 MW;  51C8A980CE79823E CRC64;
     MYNVFQMAVW LPAQNKFYLP PQPITRILST DEYVTRTNLF YHATSERLLL VGHPLFEISS
     NQTVTIPKVS PNAFRVFRVR FADPNRFAFG DKAIFNPETE RLVWGLRGIE IGRGQPLGIG
     ITGHPLLNKL DDAENPTNYI NTHANGDSRQ NTAFDAKQTQ MFLVGCTPAS GEHWTSSRCP
     GEQVKLGDCP RVQMIESVIE DGDMMDIGFG AMDFAALQQD KSDVPLDVVQ ATCKYPDYIR
     MNHEAYGNSM FFFARREQMY TRHFFTRGGS VGDKEAVPQS LYLTADAEPR TTLATTNYVG
     TPSGSMVSSD VQLFNRSYWL QRCQGQNNGI CWRNQLFITV GDNTRGTSLS ISMKNNASTT
     YSNANFNDFL RHTEEFDLSF IVQLCKVKLT PENLAYIHTM DPNILEDWQL SVSQPPTNPL
     EDQYRFLGSS LAAKCPEQAP PEPQTDPYSQ YKFWEVDLTE RMSEQLDQFP LGRKFLYQSG
     MTQRTATSST TKRKTVRVST SAKRRRKA